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Protein

Alpha-crystallin B chain

Gene

CRYAB

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Zinc 1By similarity
Metal bindingi104 – 1041Zinc 2By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi111 – 1111Zinc 1By similarity
Metal bindingi119 – 1191Zinc 1By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
Gene namesi
Name:CRYAB
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Alpha-crystallin B chainPRO_0000125912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei22 – 221Omega-N-methylated arginineBy similarity
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei50 – 501Omega-N-methylated arginineBy similarity
Modified residuei59 – 591Phosphoserine1 Publication
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei166 – 1661N6-acetyllysineBy similarity
Glycosylationi170 – 1701O-linked (GlcNAc)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

PTM databases

iPTMnetiP41316.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Interactioni

Subunit structurei

Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin. Interacts with TMEM109.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000011163.

Structurei

3D structure databases

ProteinModelPortaliP41316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP41316.
KOiK09542.
OMAiTITAPMK.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR
60 70 80 90 100
PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV
110 120 130 140 150
HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK
160 170
QAPGPERTIP ITREEKPAVT AAPKK
Length:175
Mass (Da):20,107
Last modified:February 1, 1995 - v1
Checksum:i636FBAB9D6CE90D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95383 mRNA. Translation: CAA64669.1.
PIRiA53871.
RefSeqiNP_001075876.1. NM_001082407.1.
UniGeneiOcu.6416.

Genome annotation databases

GeneIDi100009295.
KEGGiocu:100009295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95383 mRNA. Translation: CAA64669.1.
PIRiA53871.
RefSeqiNP_001075876.1. NM_001082407.1.
UniGeneiOcu.6416.

3D structure databases

ProteinModelPortaliP41316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000011163.

PTM databases

iPTMnetiP41316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009295.
KEGGiocu:100009295.

Organism-specific databases

CTDi1410.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP41316.
KOiK09542.
OMAiTITAPMK.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure of rabbit lens alpha-crystallins."
    Parveen R., Smith J.B., Sun Y., Smith D.L.
    J. Protein Chem. 12:93-101(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lens.
  2. "Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 in lens-derived cell lines."
    Krausz E., Augusteyn R.C., Quinlan R.A., Reddan J.R., Russell P., Sax C.M., Graw J.
    Invest. Ophthalmol. Vis. Sci. 37:2120-2128(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.

Entry informationi

Entry nameiCRYAB_RABIT
AccessioniPrimary (citable) accession number: P41316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 20, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.